• Molecular basis for receptor tyrosine kinase A-loop tyrosine transphosphorylation

    24 days ago - By ACS Division of Biological Chemistry

    Nature Chemical Biology, Published online: 20 January 2020; doi:10.1038/s41589-019-0455-7 X-ray crystallography, solution NMR and biochemical and cell-based analyses reveal a model where catalytically repressed receptor tyrosine kinases accomplish activation loop tyrosine transphosphorylation.
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  • Structural equilibrium underlying ligand-dependent activation of β 2 -adrenoreceptor

    24 days ago - By ACS Division of Biological Chemistry

    Nature Chemical Biology, Published online: 20 January 2020; doi:10.1038/s41589-019-0457-5 NMR structural analysis of an active state of the β2-adrenergic receptor defines a unique orientation for the intracellular half of TM6, responsible for G-protein binding, including an equilibrium among three conformations of a key microswitch.
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  • Biased modulators of NMDA receptors control channel opening and ion selectivity

    24 days ago - By ACS Division of Biological Chemistry

    Nature Chemical Biology, Published online: 20 January 2020; doi:10.1038/s41589-019-0449-5 A series of positive allosteric modulators of NMDA receptors that can increase agonist potency, increase channel-open probability, and slow receptor deactivation can also decrease single-channel conductance and decrease calcium permeability.
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